1. Mydj2 as a potent partner of hsc70 in mammalian cells.
- Author
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Bozidis P, Lazaridis I, Pagoulatos GN, and Angelidis CE
- Subjects
- Animals, Carrier Proteins genetics, Cell Nucleus metabolism, Cells, Cultured, DNA, Complementary isolation & purification, HSC70 Heat-Shock Proteins, HSP40 Heat-Shock Proteins, Haplorhini, Heat-Shock Proteins genetics, Male, Mice, RNA, Messenger analysis, Carrier Proteins metabolism, HSP70 Heat-Shock Proteins metabolism, Heat-Shock Proteins metabolism
- Abstract
Dj2 is a member of the DnaJ family of proteins, which regulate the chaperoning function of the hsp70s. We isolated a monkey cDNA dj2 clone corresponding to the large mRNA species encoded by the gene. This mRNA differs from the small mRNA produced by the same gene in that it contains a long 3' untranslated region. Both messages were found to be equally stable and to produce the same protein, which is susceptible to farnesylation. Studies in mouse tissues and various cell lines revealed that these messages and their products are differentially expressed. Surprisingly, we found that only the nonfarnesylated form of dj2 is capable of translocating to the cell nucleus, especially after heat shock. Finally, based on protein interaction studies, our results indicate that dj2 is a specific partner for hsc70 and not for hsp70.
- Published
- 2002
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